Double cross-validation and improved sensitivity of the rapid screen of mild traumatic brain injury

This study aimed to replicate and cross-validate the Rapid Screen of Concussion (RSC) for diagnosing mild TBI (mTBI). One hundred (81 male, 19 female) cases of mTBI and 35 (23 male and 12 female) cases of orthopaedic injuries were tested within 24 hr of injury. Double cross-validation was used to examine whether total RSC scores obtained in the cur-rent sample, generalised to one previously reported. In the new sample, mTBI patients answered fewer orientation questions, recalled fewer words on the learning trial and after a delay, judged fewer sentences in 2 min, and completed fewer symbols in the Digit Symbol Substitution Test than orthopaedic controls. The formulae and cut-offs developed on the original and new samples produced similar sensitivity and overall correct classification rates. Inclusion of the Digit Symbol Substitution Test performance of the new sample improved the sensitivity (80.2%) and specificity (82.6%) in males. It did not improve the correct classification rate in females, which was 89.5% sensitivity and 91.7% specificity before the inclusion of the Digit Symbol Substitution Test. Taken together, these results indicate that a combined score on this 12-min screen yields a measure of level of brain impairment up to 24 hr after mTBI.

The cross-entropy method for network reliability estimation

Consider a network of unreliable links, modelling for example a communication network. Estimating the reliability of the network-expressed as the probability that certain nodes in the network are connected-is a computationally difficult task. In this paper we study how the Cross-Entropy method can be used to obtain more efficient network reliability estimation procedures. Three techniques of estimation are considered: Crude Monte Carlo and the more sophisticated Permutation Monte Carlo and Merge Process. We show that the Cross-Entropy method yields a speed-up over all three techniques.

Modelling the structure of latexin-carboxypeptidase A complex based on chemical cross-linking and molecular docking

We have determined the three-dimensional structure of the protein complex between latexin and carboxypeptidase A using a combination of chemical cross-linking, mass spectrometry and molecular docking. The locations of three intermolecular cross-links were identified using mass spectrometry and these constraints were used in combination with a speed-optimised docking algorithm allowing us to evaluate more than 3 x 10(11) possible conformations. While cross-links represent only limited structural constraints, the combination of only three experimental cross-links with very basic molecular docking was sufficient to determine the complex structure. The crystal structure of the complex between latexin and carboxypeptidase A4 determined recently allowed us to assess the success of this structure determination approach. Our structure was shown to be within 4 angstrom r.m.s. deviation of C alpha atoms of the crystal structure. The study demonstrates that cross-linking in combination with mass spectrometry can lead to efficient and accurate structural modelling of protein complexes.